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| | ==Crystal structure of FimX GGDEF domain from Pseudomonas aeruginosa== | | ==Crystal structure of FimX GGDEF domain from Pseudomonas aeruginosa== |
| - | <StructureSection load='3hva' size='340' side='right' caption='[[3hva]], [[Resolution|resolution]] 2.04Å' scene=''> | + | <StructureSection load='3hva' size='340' side='right'caption='[[3hva]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hva]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HVA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hv8|3hv8]], [[3hv9|3hv9]], [[3hvb|3hvb]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.042Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimX, PA4959 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hva OCA], [https://pdbe.org/3hva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hva RCSB], [https://www.ebi.ac.uk/pdbsum/3hva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hva ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diguanylate_cyclase Diguanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.65 2.7.7.65] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hva OCA], [http://pdbe.org/3hva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hva RCSB], [http://www.ebi.ac.uk/pdbsum/3hva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hva ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9HUK6_PSEAE Q9HUK6_PSEAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diguanylate cyclase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Bae, N]] | + | [[Category: Bae N]] |
| - | [[Category: De, N]] | + | [[Category: De N]] |
| - | [[Category: Navarro, M V.A S]] | + | [[Category: Navarro MVAS]] |
| - | [[Category: Sondermann, H]] | + | [[Category: Sondermann H]] |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: C-di-gmp]]
| + | |
| - | [[Category: Ggdef diguanylate cyclase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9HUK6_PSEAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial pathogenesis involves social behavior including biofilm formation and swarming, processes that are regulated by the bacterially unique second messenger cyclic di-GMP (c-di-GMP). Diguanylate cyclases containing GGDEF and phosphodiesterases containing EAL domains have been identified as the enzymes controlling cellular c-di-GMP levels, yet less is known regarding signal transmission and the targets of c-di-GMP. FimX, a protein from Pseudomonas aeruginosa that governs twitching motility, belongs to a large subfamily containing both GGDEF and EAL domains. Biochemical and structural analyses reveals its function as a high-affinity receptor for c-di-GMP. A model for full-length FimX was generated combining solution scattering data and crystal structures of the degenerate GGDEF and EAL domains. Although FimX forms a dimer in solution via the N-terminal domains, a crystallographic EAL domain dimer suggests modes for the regulation of FimX by c-di-GMP binding. The results provide the structural basis for c-di-GMP sensing via degenerate phosphodiesterases.
Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.,Navarro MV, De N, Bae N, Wang Q, Sondermann H Structure. 2009 Aug 12;17(8):1104-16. PMID:19679088[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Navarro MV, De N, Bae N, Wang Q, Sondermann H. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure. 2009 Aug 12;17(8):1104-16. PMID:19679088 doi:10.1016/j.str.2009.06.010
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